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Sialylated carbohydrate chains of recombinant human glycoproteins expressed in Chinese hamster ovary cells contain traces of N ‐glycolylneuraminic acid
Author(s) -
Hokke Cornelis H.,
Bergwerff Aldert A.,
van Dedem Gijs W.K.,
van Oostrum Jan,
Kamerling Johannis P.,
Vliegenthart Johannis F.G.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81427-p
Subject(s) - chinese hamster ovary cell , sialic acid , recombinant dna , glycoprotein , biochemistry , chemistry , plasminogen activator , chimera (genetics) , microbiology and biotechnology , neuraminic acid , biology , gene , receptor , endocrinology
HPLC analysis of sialic acid released from recombinant variants of human tissue plasminogen activator, human chimeric plasminogen activator, human erythropoietin, and human follitropin, expressed in Chinese hamster ovary cells, demonstrates for each glycoprotein the presence of N ‐acetylneuraminic and N ‐glycolylneuraminic acid in a ratio of 97:3. Structural analysis by 500 MHz 1 H‐NMR spectroscopy, of the enzymatically released N‐linked carbohydrate chains of chimeric plasminogen activator and of erythropoietin, showed that α2‐3 linked N ‐glycolylneuraminic acid can occur in different N ‐acetyllactosamine type antennary structures.